Unknown

Dataset Information

0

Diversity of Short Linear Interaction Motifs in SARS-CoV-2 Nucleocapsid Protein.


ABSTRACT: Molecular mimicry of short linear interaction motifs has emerged as a key mechanism for viral proteins binding host domains and hijacking host cell processes. Here, we examine the role of RNA-virus sequence diversity in the dynamics of the virus-host interface, by analyzing the uniquely vast sequence record of viable SARS-CoV-2 species with focus on the multi-functional nucleocapsid protein. We observe the abundant presentation of motifs encoding several essential host protein interactions, alongside a majority of possibly non-functional and randomly occurring motif sequences absent in subsets of viable virus species. A large number of motifs emerge ex nihilo through transient mutations relative to the ancestral consensus sequence. The observed mutational landscape implies an accessible motif space that spans at least 25% of known eukaryotic motifs. This reveals motif mimicry as a highly dynamic process with the capacity to broadly explore host motifs, allowing the virus to rapidly evolve the virus-host interface.

SUBMITTER: Schuck P 

PROVIDER: S-EPMC10542142 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Diversity of Short Linear Interaction Motifs in SARS-CoV-2 Nucleocapsid Protein.

Schuck Peter P   Zhao Huaying H  

bioRxiv : the preprint server for biology 20230801


Molecular mimicry of short linear interaction motifs has emerged as a key mechanism for viral proteins binding host domains and hijacking host cell processes. Here, we examine the role of RNA-virus sequence diversity in the dynamics of the virus-host interface, by analyzing the uniquely vast sequence record of viable SARS-CoV-2 species with focus on the multi-functional nucleocapsid protein. We observe the abundant presentation of motifs encoding several essential host protein interactions, alon  ...[more]

Similar Datasets

| S-EPMC10746173 | biostudies-literature
| S-EPMC1665647 | biostudies-literature
| S-EPMC10327126 | biostudies-literature
| S-EPMC4654906 | biostudies-literature
| S-EPMC9794558 | biostudies-literature
| S-EPMC4670012 | biostudies-literature
| S-EPMC11318550 | biostudies-literature
| S-EPMC8315091 | biostudies-literature
| S-EPMC5345135 | biostudies-literature
| S-EPMC11539619 | biostudies-literature